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E. coli persists against antibiotics through HipA-induced dormancy
Date:1/15/2009

ll, for example," Brennan explains. To function, a protein must be able to close down on its target molecules - called substrates. The closed state is the active state.
  • HipB also might physically sequester HipA from EF-Tu because the HipA/HipB/DNA complex is located in E. coli's nucleoid, far from the bacteria's membrane where EF-Tu is mainly found.
  • HipA is free to cause trouble when its ties to HipB are broken; an infrequent occurrence which the authors note is likely caused by proteases tugging the smaller and structurally vulnerable HipB protein out of the complex.

    Protein kinases often bind to more than one protein, so there are likely multiple targets for the protein in E. coli and other gram-negative bacteria, Schumacher and Brennan said.

    Future research will focus on finding other HipA targets in E. coli, and kinase inhibitors will be examined for their ability to affect HipA function. If a promising inhibitor is found, its structure will be solved to clarify its binding mode and how it might be tweaked to bind HipA even better. "Structure-based drug design should provide the best chance at formulating highly specific and effective drugs against HipA," Schumacher said.


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    Contact: Scott Merville
    smerville@mdanderson.org
    713-792-0661
    University of Texas M. D. Anderson Cancer Center
    Source:Eurekalert  

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